Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay
| Autor: | A Datta, T. K. Kirk, Alan D. Bettermann |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Blotting
Western Molecular Sequence Data engineering.material Lignin Applied Microbiology and Biotechnology Fungal Proteins chemistry.chemical_compound Manganese peroxidase Amino Acid Sequence chemistry.chemical_classification Ecology biology Basidiomycota Pulp (paper) Lignin peroxidase Chromatography Ion Exchange biology.organism_classification Wood Amino acid Alcohol Oxidoreductases Kinetics Biodegradation Environmental Peroxidases chemistry Biochemistry Xylanase biology.protein engineering Phanerochaete Research Article Food Science Biotechnology Peroxidase |
| Zdroj: | Applied and Environmental Microbiology. 57:1453-1460 |
| ISSN: | 1098-5336 0099-2240 |
| DOI: | 10.1128/aem.57.5.1453-1460.1991 |
| Popis: | The specific enzymes associated with lignin degradation in solid lignocellulosic substrates have not been identified. Therefore, we examined extracts of cultures of Phanerochaete chrysosporium that were degrading a mechanical pulp of aspen wood. Western blot (immunoblot) analyses of the partially purified protein revealed lignin peroxidase, manganese-dependent peroxidase (MnP), and glyoxal oxidase. The dominant peroxidase, an isoenzyme of MnP (pI 4.9), was isolated, and its N-terminal amino acid sequence and amino acid composition were determined. The results reveal both similarities to and differences from the deduced amino acid sequences from cDNA clones of dominant MnP isoenzymes from liquid cultures. Our results suggest, therefore, that the ligninolytic-enzyme-encoding genes that are expressed during solid substrate degradation differ from those expressed in liquid culture or are allelic variants of their liquid culture counterparts. In addition to lignin peroxidase, MnP, and glyoxal oxidase, xylanase and protease activities were present in the extracts of the degrading pulp. |
| Databáze: | OpenAIRE |
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